Abstract

Protein oxidation is a topic of indisputable scientific interest given the impact of oxidized proteins on food quality and safety. Carbonylation is regarded as one of the most notable post-translational modifications in proteins and yet, this reaction and its consequences are poorly understood. From a mechanistic perspective, primary protein carbonyls (i.e. α-aminoadipic and γ-glutamic semialdehydes) have been linked to radical-mediated oxidative stress, but recent studies emphasize the role alternative carbonylation pathways linked to the Maillard reaction. Secondary protein carbonyls are introduced in proteins via covalent linkage of lipid carbonyls (i.e. protein-bound malondialdehyde). The high reactivity of protein carbonyls in foods and other biological systems indicates the intricate chemistry of these species and urges further research to provide insight into these molecular mechanisms and pathways. In particular, protein carbonyls are involved in the formation of aberrant and dysfunctional protein aggregates, undergo further oxidation to yield carboxylic acids of biological relevance and establish interactions with other biomolecules such as oxidizing lipids and phytochemicals. From a methodological perspective, the routine dinitrophenylhydrazine (DNPH) method is criticized not only for the lack of accuracy and consistency but also authors typically perform a poor interpretation of DNPH results, which leads to misleading conclusions. From a practical perspective, the biological relevance of protein carbonyls in the field of food science and nutrition is still a topic of debate. Though the implication of carbonylation on impaired protein functionality and poor protein digestibility is generally recognized, the underlying mechanism of such connections requires further clarification. From a medical perspective, protein carbonyls are highlighted as markers of protein oxidation, oxidative stress and disease. Yet, the specific role of specific protein carbonyls in the onset of particular biological impairments needs further investigations. Recent studies indicates that regardless of the origin (in vivo or dietary) protein carbonyls may act as signalling molecules which activate not only the endogenous antioxidant defences but also implicate the immune system. The present paper concisely reviews the most recent advances in this topic to identify, when applicable, potential fields of interest for future studies.

Highlights

  • Oxidative stress is a major cause of post-translational changes in proteins and includes severe chemical modifications such as aggregation via protein crosslinks and fragmentations via peptide scission (Davies 2016; Kehm et al 2021)

  • The α-aminoadipic semialdehyde (α-AS) is a specific oxidation product from lysine and account for up to the 70% of total protein carbonyls in cells (Requena et al 2001) and food systems (Estévez 2011). Owing to their ubiquity in oxidized proteins and their simple detection and quantification by the routine dinitrophenylhydrazine (DNPH) method, protein carbonyls have been emphasized as general markers of protein oxidation in foods, cells and tissues (Estévez 2011; Hellwig 2020)

  • The recent advances achieved in the field of protein carbonylation facilitate the understanding of the biological significance of this multifaceted reaction

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Summary

Introduction

Oxidative stress is a major cause of post-translational changes in proteins and includes severe chemical modifications such as aggregation via protein crosslinks and fragmentations via peptide scission (Davies 2016; Kehm et al 2021). Recent studies have reported innovative evidence on the toxicological effects of dietary protein carbonyls and other oxidized amino acids (Estévez and Xiong 2019) and the role of these compounds in cell signalling mechanisms (Wong et al 2012; Kehm et al 2021).

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